Analysis of multiple guanine exchange factors shows that Rab activation can occur via a number of mechanistically distinct GDP-release pathways.

The dynein light intermediate chain is a member of the G protein superfamily and links the motor to several intracellular cargo adaptors.

Relocation of Rab, Ras and Rho family GTPases to the surface of mitochondria enables efficient identification of their effectors, exchange factors and GAPs by proximity biotinylation.

A systems level reconstitution of H-Ras GTPase signaling reveals a rich space of tunable dynamic outputs and clarifies the consequences of oncogenic perturbations to signaling.

The important oncogene KRasG13C can be targeted by covalently binding nucleotide-analogues, resulting in a locked protein that can no longer induce oncogenic signaling.

Sequence conservation in Ras depends strongly on the biochemical network in which it operates, providing a framework for understanding the origin of global selection pressures on proteins.

Deep mutagenesis experiments demonstrate that while cancer-causing mutations in Ras selectively alter regulatory interactions with GTPase-activating proteins, Ras is also activated by many mutations that decrease protein stability.

Palmitate turnover is controlled by distinct enzyme families with different specificities.

Myostatin signaling governs neonatal longitudinal muscle growth and neuromuscular contractures in a sex-dependent manner, identifying a potential avenue for contracture treatment and underscoring the need to consider sex as a biological variable in the pathophysiology of acquired neuromuscular disorders.

A posttranslational regulatory mechanism for a Ras family small GTPase could open up new directions to understand and control the Ras family of proteins that are important for physiology and diseases.